SARS-unique fold in the Rousettus bat coronavirus HKU9.
Identifieur interne : 000B18 ( PubMed/Corpus ); précédent : 000B17; suivant : 000B19SARS-unique fold in the Rousettus bat coronavirus HKU9.
Auteurs : Robert G. Hammond ; Xuan Tan ; Margaret A. JohnsonSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2017.
English descriptors
- KwdEn :
- Animals, Chiroptera, Coronavirus (chemistry), Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Domains, Protein Folding, RNA Replicase (chemistry), RNA Replicase (metabolism), SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : RNA Replicase, Viral Nonstructural Proteins.
- chemistry : Coronavirus, SARS Virus.
- chemical , metabolism : RNA Replicase, Viral Nonstructural Proteins.
- Animals, Chiroptera, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Domains, Protein Folding.
Abstract
The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.
DOI: 10.1002/pro.3208
PubMed: 28580734
Links to Exploration step
pubmed:28580734Le document en format XML
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Johnson</name><affiliation><nlm:affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28580734</idno><idno type="pmid">28580734</idno><idno type="doi">10.1002/pro.3208</idno><idno type="wicri:Area/PubMed/Corpus">000B18</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B18</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">SARS-unique fold in the Rousettus bat coronavirus HKU9.</title><author><name sortKey="Hammond, Robert G" sort="Hammond, Robert G" uniqKey="Hammond R" first="Robert G" last="Hammond">Robert G. Hammond</name><affiliation><nlm:affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</nlm:affiliation></affiliation></author><author><name sortKey="Tan, Xuan" sort="Tan, Xuan" uniqKey="Tan X" first="Xuan" last="Tan">Xuan Tan</name><affiliation><nlm:affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</nlm:affiliation></affiliation></author><author><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name><affiliation><nlm:affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="eISSN">1469-896X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Chiroptera</term><term>Coronavirus (chemistry)</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Domains</term><term>Protein Folding</term><term>RNA Replicase (chemistry)</term><term>RNA Replicase (metabolism)</term><term>SARS Virus (chemistry)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chiroptera</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Domains</term><term>Protein Folding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28580734</PMID><DateCompleted><Year>2017</Year><Month>09</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-896X</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>9</Issue><PubDate><Year>2017</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Protein science : a publication of the Protein Society</Title><ISOAbbreviation>Protein Sci.</ISOAbbreviation></Journal><ArticleTitle>SARS-unique fold in the Rousettus bat coronavirus HKU9.</ArticleTitle><Pagination><MedlinePgn>1726-1737</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/pro.3208</ELocationID><Abstract><AbstractText>The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.</AbstractText><CopyrightInformation>© 2017 The Protein Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hammond</LastName><ForeName>Robert G</ForeName><Initials>RG</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Xuan</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Margaret A</ForeName><Initials>MA</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-4422-399X</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R35 GM119456</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>06</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Protein Sci</MedlineTA><NlmUniqueID>9211750</NlmUniqueID><ISSNLinking>0961-8368</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural 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